Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp)4-Lys-Ile-Val-Gly and its analogs.

نویسندگان

  • Yong-Tae Kim
  • Wataru Nishii
  • Masashi Matsushima
  • Hideshi Inoue
  • Hisashi Ito
  • Sun Joo Park
  • Kenji Takahashi
چکیده

The substrate specificities of porcine and bovine enteropeptidases were investigated using the peptide Val-(Asp)(4)-Lys-Ile-Val-Gly and its various analogs with mutations in the (Asp)(4)-Lys sequence as substrates. The results indicated that in addition to P1 Lys, P2 Asp in the substrates is most important, that P3 Asp is additionally important, and that P5 Asp contributes somewhat to the susceptibility, and that P4 Asp is the least important. These results were essentially identical as between porcine and bovine enteropeptidases.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

N-Ac-Ser-Asn-Lys-Phe-Leu-Gly-Thr- Trp-Lys-Leu-Val-Ser-Ser-Glu-Asn-Phe-Asp-Asp-Tyr- Met-Lys-Ala-Leu-Gly-Val-Gly-Leu-Ala-Thr-Arg-Lys- Leu-Gly-Asn-Leu-Ala-Lys-Pro-Asn-Val-Ile-Ile-Ser- Lys-Lys-Gly-Asp-Ile-Ile-Thr-Ile-Arg-Thr-Glu-Ser-Gly-

The reaction of the P2 protein from rabbit sciatic nerve with CNBr produced four peptides: a 20-residue peptide (CN3) containing tryptophan which occupies the blocked NHZ terminus; Peptide CN1, a large peptide comprising over 70% of the P2 molecule; Peptide CN2, a fraction containing two tightly bound peptides having 2 half-cystine residues and comprising the COOH terminus; and Peptide CN4, a n...

متن کامل

N-Ac-Ser-Asn-Lys-Phe-Leu-Gly-Thr- Trp-Lys-Leu-Val-Ser-Ser-Glu-Asn-Phe-Asp-Asp-Tyr- Met-Lys-Ala-Leu-Gly-Val-Gly-Leu-Ala-Thr-Arg-Lys- Leu-Gly-Asn-Leu-Ala-Lys-Pro-Asn-Val-Ile-Ile-Ser-

The reaction of the P2 protein from rabbit sciatic nerve with CNBr produced four peptides: a 20-residue peptide (CN3) containing tryptophan which occupies the blocked NHZ terminus; Peptide CN1, a large peptide comprising over 70% of the P2 molecule; Peptide CN2, a fraction containing two tightly bound peptides having 2 half-cystine residues and comprising the COOH terminus; and Peptide CN4, a n...

متن کامل

The covalent structure of pig kidney fructose-1,6-bisphosphatase. Sequence of a 63-residue cyanogen bromide peptide containing a phosphorylatable serine.

Native pig kidney fructose-1,6-bisphosphatase, in contrast to the rat liver enzyme, is not a substrate of cyclic AMP-dependent protein kinase. However, the pig kidney enzyme becomes a substrate when phosphorylation is performed in 1.6 M urea, after prior unfolding in 8 M urea. A cyanogen bromide fragment containing the phosphorylation site has been isolated and the amino acid sequence of this 6...

متن کامل

Classical diphtheria caused by Corynebacterium ulcerans in Germany: amino acid sequence differences between diphtheria toxins from Corynebacterium diphtheriae and C. ulcerans.

2 Ser Asn Asn Asn 14 Leu Ile Leu Leu 22 Ser Ser Leu Leu 31 Val Asp Val Val 67 Thr Ala Thr Ala 116 Val Ile Ile Ile 183 Ala Ala Glu Glu 210 Ala Ser Ser Ser 233 Val Ala Ala Ala 262 Thr Ile Thr Thr 277 Gln Gln Arg Gln 294 Thr Val Val Val 296 Pro Ser Ser Ser 305 Ala Ser Ser Ser 314 Ile Val Val Val 317 Glu Lys Lys Lys 378 Ile Leu Leu Leu 415 Leu Val Val Val 417 Asp Gly Gly Gly 421 Val Ala Ala Ala 432...

متن کامل

Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus.

Five structurally related heptadecapeptides rich in hydrophobic amino acids have been discovered in the venom of the bumblebee Megabombus pennsylvanicus. We have named them bombolitin I (Ile-Lys-Ile-Thr-Thr-Met-Leu-Ala-Lys-Leu-Gly-Lys-Val-Leu-Ala-His-Val-NH2 ), bombolitin II (Ser-Lys-Ile-Thr-Asp-Ile-Leu-Ala-Lys-Leu-Gly-Lys-Val-Leu-Ala-His-Val-NH2 ), bombolitin III (Ile-Lys-Ile-Met-Asp-Ile-Leu-A...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Bioscience, biotechnology, and biochemistry

دوره 72 3  شماره 

صفحات  -

تاریخ انتشار 2008